An x-ray absorption spectroscopy study of the zinc environment in Langmuir-Blodgett phospholipid multilayers.
An x-ray absorption spectroscopy study of the zinc environment in Langmuir-Blodgett phospholipid multilayers.
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DOI：
10.1016/s0006-3495(02)75350-2
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发表时间：
2002-12
影响因子：
3.4
通讯作者：
S. Nuzzo;Carlo Meneghini;S. Mobilioo;Heinrich Haas;Paolo Riccio;A. Fasano;P. Cavatorta;Silvia Morante
中科院分区：
文献类型：
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作者：
S. Nuzzo;Carlo Meneghini;S. Mobilioo;Heinrich Haas;Paolo Riccio;A. Fasano;P. Cavatorta;Silvia Morante
第一次X射线吸收光谱被用来调查的Zn环境中的LB多层膜。该多层被视为髓鞘的多层结构的模型，髓鞘是围绕神经轴突的膜，其在沿着轴突的信号传导中起着至关重要的作用。在存在和不存在髓鞘碱性蛋白的情况下，从磷脂二月桂酰磷脂酸组装层。的扩展的X-射线吸收精细结构和X-射线吸收光谱在Zn K-边缘的近边缘区域的分析提供了一个准确的描述的局部结构，表明Zn离子绑定到磷脂分子的头部。的髓鞘碱性蛋白诱导的扭曲Zn局部环境由于空间的约束，但不取代磷酸头基。这些发现代表了理解髓鞘碱性蛋白、锌和髓鞘脂质之间相互作用的重要一步。
For the first time x-ray absorption spectroscopy was used to investigate the Zn environment in Langmuir-Blodgett multilayers. The multilayers were taken as a model of the multilamellar structure of the myelin sheath, the membrane surrounding the nerve axon, which plays a crucial role for signal transduction along the axon. The layers were assembled from the phospholipid dilauroylphosphatidic acid, both in the presence and in the absence of myelin basic protein. The analysis of the extended x-ray absorption fine structure and of the near edge regions of the x-ray absorption spectra at the Zn K-edge provided an accurate description of the local structure showing that the Zn ions are bound to the heads of the phospholipid molecules. The myelin basic protein induces a distortion on the Zn local environment due to a steric constraint but does not substitute the phosphate headgroups. These findings represent an important step in understanding the interplay among myelin basic protein, Zn, and the lipids of the myelin sheath.